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• W2021825316 startingPage "1310" @default.
• W2021825316 abstract "Activation domains are functional modules that enable sequence-specific DNA binding proteins to stimulate transcription. The structural basis for the function of activation domains is poorly understood. A combination of nuclear magnetic resonance (NMR) and biochemical experiments revealed that the minimal acidic activation domain of the herpes simplex virus VP16 protein undergoes an induced transition from random coil to α helix upon binding to its target protein, hTAF II 31 (a human TFIID TATA box – binding protein-associated factor). Identification of the two hydrophobic residues that make nonpolar contacts suggests a general recognition motif of acidic activation domains for hTAF II 31." @default.
• W2021825316 created "2016-06-24" @default.
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• W2021825316 date "1997-08-29" @default.
• W2021825316 modified "2023-10-16" @default.
• W2021825316 title "Induced α Helix in the VP16 Activation Domain upon Binding to a Human TAF" @default.
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• W2021825316 doi "https://doi.org/10.1126/science.277.5330.1310" @default.
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